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Chlorine in PDB 4ua3: Crystal Structure of Selenomethionine Labeled Spnatd

Protein crystallography data

The structure of Crystal Structure of Selenomethionine Labeled Spnatd, PDB code: 4ua3 was solved by R.S.Magin, G.P.Liszczak, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.36 / 1.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.701, 42.629, 85.417, 90.00, 98.68, 90.00
R / Rfree (%) 17.9 / 23.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Selenomethionine Labeled Spnatd (pdb code 4ua3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Selenomethionine Labeled Spnatd, PDB code: 4ua3:

Chlorine binding site 1 out of 1 in 4ua3

Go back to Chlorine Binding Sites List in 4ua3
Chlorine binding site 1 out of 1 in the Crystal Structure of Selenomethionine Labeled Spnatd


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Selenomethionine Labeled Spnatd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:58.2
occ:1.00
N A:PHE156 3.1 52.2 1.0
ND2 A:ASN159 3.2 55.0 1.0
CG2 A:VAL155 3.5 51.2 1.0
C2P A:COA301 3.5 59.5 1.0
O A:HOH418 3.6 70.2 1.0
CD2 A:PHE156 3.7 58.4 1.0
CA A:VAL155 3.7 53.0 1.0
CE A:MSE60 3.8 73.8 1.0
CB A:ASN159 3.8 56.3 1.0
CB A:PHE156 3.9 53.6 1.0
C A:VAL155 3.9 53.6 1.0
CG A:ASN159 4.0 57.4 1.0
CA A:PHE156 4.1 54.5 1.0
CG A:PHE156 4.1 56.6 1.0
CB A:VAL155 4.2 51.9 1.0
C3P A:COA301 4.5 55.9 1.0
CE2 A:PHE156 4.5 59.3 1.0
O A:PHE156 4.6 57.9 1.0
O A:THR154 4.7 49.3 1.0
S1P A:COA301 4.8 64.5 1.0
C A:PHE156 4.9 55.1 1.0
CB A:ALA162 4.9 58.3 1.0
N A:VAL155 5.0 49.8 1.0
CD1 A:LEU63 5.0 65.1 1.0

Reference:

R.S.Magin, G.P.Liszczak, R.Marmorstein. The Molecular Basis For Histone H4- and H2A-Specific Amino-Terminal Acetylation By Natd. Structure V. 23 332 2015.
ISSN: ISSN 0969-2126
PubMed: 25619998
DOI: 10.1016/J.STR.2014.10.025
Page generated: Sat Dec 12 11:14:36 2020

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